5AIO
Crystal structure of t131 N-terminal TPR array
Summary for 5AIO
Entry DOI | 10.2210/pdb5aio/pdb |
Related | 5AIM |
Descriptor | TRANSCRIPTION FACTOR TAU 131 KDA SUBUNIT (1 entity in total) |
Functional Keywords | transcription, tfiiic, tprs |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
Cellular location | Nucleus : P33339 |
Total number of polymer chains | 1 |
Total formula weight | 52437.97 |
Authors | Male, G.,Glatt, S.,Mueller, C.W. (deposition date: 2015-02-16, release date: 2015-06-24, Last modification date: 2024-05-08) |
Primary citation | Male, G.,von Appen, A.,Glatt, S.,Taylor, N.M.,Cristovao, M.,Groetsch, H.,Beck, M.,Muller, C.W. Architecture of TFIIIC and its role in RNA polymerase III pre-initiation complex assembly. Nat Commun, 6:7387-7387, 2015 Cited by PubMed Abstract: In eukaryotes, RNA Polymerase III (Pol III) is specifically responsible for transcribing genes encoding tRNAs and other short non-coding RNAs. The recruitment of Pol III to tRNA-encoding genes requires the transcription factors (TF) IIIB and IIIC. TFIIIC has been described as a conserved, multi-subunit protein complex composed of two subcomplexes, called τA and τB. How these two subcomplexes are linked and how their interaction affects the formation of the Pol III pre-initiation complex (PIC) is poorly understood. Here we use chemical crosslinking mass spectrometry and determine the molecular architecture of TFIIIC. We further report the crystal structure of the essential TPR array from τA subunit τ131 and characterize its interaction with a central region of τB subunit τ138. The identified τ131-τ138 interacting region is essential in vivo and overlaps with TFIIIB-binding sites, revealing a crucial interaction platform for the regulation of tRNA transcription initiation. PubMed: 26060179DOI: 10.1038/ncomms8387 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.148 Å) |
Structure validation
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